ID   L0FBG6_DESDL            Unreviewed;       747 AA.
AC   L0FBG6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:AGA70370.1};
GN   OrderedLocusNames=Desdi_2963 {ECO:0000313|EMBL:AGA70370.1};
OS   Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA70370.1, ECO:0000313|Proteomes:UP000010797};
RN   [1] {ECO:0000313|Proteomes:UP000010797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA   de Vos W.M., Boon N., Smidt H., Woyke T.;
RT   "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP003344; AGA70370.1; -; Genomic_DNA.
DR   RefSeq; WP_015263331.1; NC_019903.1.
DR   AlphaFoldDB; L0FBG6; -.
DR   STRING; 871963.Desdi_2963; -.
DR   KEGG; ddl:Desdi_2963; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000010797; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR   CDD; cd02755; MopB_Thiosulfate-R-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010797}.
FT   DOMAIN          43..99
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   747 AA;  82767 MW;  E85DE8EF1E298435 CRC64;
     MRRREFLKYA LCGAGGTAIT VGSFGALNKI SPKTALATET TEEATIFSAC EMCRNQCPIA
     VKVSNGKVTK IEGNPNDSGF GGVICARGNS GPSLLYDPQR LKKPMIRTGD RGTGKYKEVS
     WDEAYTYIAE KVKEIQTTYG SEEIAFASRK GPHDMFFRAI GKGIGSPNIF SHEATCPMTR
     SVALDSMFGV EMIAADYANA KYIISFGRNW LEGIHIAQTR GIMKALAKGA KIVSLDPRLN
     VTATKGEWLP IKGATDLAFV MAMANILINE ELYDKEFVER YTSGFEQWKE AVKDKTPEWA
     EQETGIPKDT IIRVTREFAE ACPNALIEFG WRTGLTPNDY QLRRGIMIVN MMMGNFEVPG
     GYYRVKNAGV TNRFPGMTGY AKPLGSVSQP EFPKPITSRI DGTGIKGVPG QIIPEGDGAV
     GQIVESILTE SPYPIKGWFV HRFNPVISIT ESERTIEALK KLDLLVVCDL YMTDTAMYAD
     VILPECTYLE RSEQIYDMSA LTPKYVIRQA AVPLVYPDTK PAWQIYKELG ETMGIGQYFP
     YETIDDYINQ QLTPAGITLE HMKEKGVWTP EGMKPFYVRK DPLASLDNLI AKPSKKIEFY
     AEEVQQATKQ GIPQYTHYPQ PEEGQFRFVQ GKVAVHTNAG TANVPILNQL MPENSLWINP
     ESAGKLGIKD GDEIVISSGK YEHKGRAKVT QGIRPDTVFA YHGFGRISPE MKRAYGKGIN
     VNKLTDNVIG EVGNVVTSMN FVTLKKA
//